1bdo
From Proteopedia
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| - | [[Image:1bdo.gif|left|200px]] | + | [[Image:1bdo.gif|left|200px]] |
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| - | '''STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING''' | + | {{Structure |
| + | |PDB= 1bdo |SIZE=350|CAPTION= <scene name='initialview01'>1bdo</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BTN:BIOTIN'>BTN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] | ||
| + | |GENE= BIOTIN CARBOXYL CARRIER PROTEI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BDO is a [ | + | 1BDO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDO OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing., Athappilly FK, Hendrickson WA, Structure. 1995 Dec 15;3(12):1407-19. PMID:[http:// | + | Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing., Athappilly FK, Hendrickson WA, Structure. 1995 Dec 15;3(12):1407-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8747466 8747466] |
[[Category: Acetyl-CoA carboxylase]] | [[Category: Acetyl-CoA carboxylase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: selenomethionine]] | [[Category: selenomethionine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:09:37 2008'' |
Revision as of 08:09, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | BIOTIN CARBOXYL CARRIER PROTEI (Escherichia coli) | ||||||
| Activity: | Acetyl-CoA carboxylase, with EC number 6.4.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING
Overview
BACKGROUND: Acetyl-coenzyme A carboxylase catalyzes the first committed step of fatty acid biosynthesis. Universally, this reaction involves three functional components all related to a carboxybiotinyl intermediate. A biotinyl domain shuttles its covalently attached biotin prosthetic group between the active sites of a biotin carboxylase and a carboxyl transferase. In Escherichia coli, the three components reside in separate subunits: a biotinyl domain is the functional portion of one of these, biotin carboxy carrier protein (BCCP). RESULTS: We have expressed natural and selenomethionyl (Se-met) BCCP from E. coli as biotinylated recombinant proteins, proteolyzed them with subtilisin Carlsberg to produce the biotinyl domains BCCP and Se-met BCCPsc, determined the crystal structure of Se-met BCCPsc using a modified version of the multiwavelength anomalous diffraction (MAD) phasing protocol, and refined the structure for the natural BCCPsc at 1.8 A resolution. The structure may be described as a capped beta sandwich with quasi-dyad symmetry. Each half contains a characteristic hammerhead motif. The biotinylated lysin is located at a hairpin beta turn which connects the two symmetric halves of the molecule, and its biotinyl group interacts with a non-symmetric protrusion from the core. CONCLUSIONS: This first crystal structure of a biotinyl domain helps to unravel the central role of such domains in reactions catalyzed by biotin-dependent carboxylases. The hammerhead structure observed twice in BCCPsc may be regarded as the basic structural motif of biotinyl and lipoyl domains of a superfamily of enzymes. The new MAD phasing techniques developed in the course of determining this structure enhance the power of the MAD method.
About this Structure
1BDO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing., Athappilly FK, Hendrickson WA, Structure. 1995 Dec 15;3(12):1407-19. PMID:8747466
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